3q87

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Current revision (08:34, 20 March 2024) (edit) (undo)
 
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<StructureSection load='3q87' size='340' side='right'caption='[[3q87]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3q87' size='340' side='right'caption='[[3q87]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3q87]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enccn Enccn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q87 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q87 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3q87]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Encephalitozoon_cuniculi Encephalitozoon cuniculi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q87 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q87 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.997&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2j6a|2j6a]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3q87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q87 OCA], [https://pdbe.org/3q87 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q87 RCSB], [https://www.ebi.ac.uk/pdbsum/3q87 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q87 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3q87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q87 OCA], [https://pdbe.org/3q87 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q87 RCSB], [https://www.ebi.ac.uk/pdbsum/3q87 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q87 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q8SUP0_ENCCU Q8SUP0_ENCCU]
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Methylation is a common modification encountered in DNA, RNA and proteins. It plays a central role in gene expression, protein function and mRNA translation. Prokaryotic and eukaryotic class I translation termination factors are methylated on the glutamine of the essential and universally conserved GGQ motif, in line with an important cellular role. In eukaryotes, this modification is performed by the Mtq2-Trm112 holoenzyme. Trm112 activates not only the Mtq2 catalytic subunit but also two other tRNA methyltransferases (Trm9 and Trm11). To understand the molecular mechanisms underlying methyltransferase activation by Trm112, we have determined the 3D structure of the Mtq2-Trm112 complex and mapped its active site. Using site-directed mutagenesis and in vivo functional experiments, we show that this structure can also serve as a model for the Trm9-Trm112 complex, supporting our hypothesis that Trm112 uses a common strategy to activate these three methyltransferases.
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Mechanism of activation of methyltransferases involved in translation by the Trm112 'hub' protein.,Liger D, Mora L, Lazar N, Figaro S, Henri J, Scrima N, Buckingham RH, van Tilbeurgh H, Heurgue-Hamard V, Graille M Nucleic Acids Res. 2011 Apr 7. PMID:21478168<ref>PMID:21478168</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3q87" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Enccn]]
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[[Category: Encephalitozoon cuniculi]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Buckingham, R H]]
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[[Category: Buckingham RH]]
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[[Category: Figaro, S]]
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[[Category: Figaro S]]
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[[Category: Graille, M]]
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[[Category: Graille M]]
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[[Category: Henri, J]]
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[[Category: Henri J]]
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[[Category: Heurgue-Hamard, V]]
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[[Category: Heurgue-Hamard V]]
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[[Category: Lazar, N]]
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[[Category: Lazar N]]
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[[Category: Liger, D]]
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[[Category: Liger D]]
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[[Category: Mora, L]]
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[[Category: Mora L]]
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[[Category: Scrima, N]]
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[[Category: Scrima N]]
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[[Category: Tilbeurgh, H van]]
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[[Category: Van Tilbeurgh H]]
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[[Category: Methylation]]
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[[Category: Methyltransferase]]
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[[Category: Sam-methyltransferase]]
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[[Category: Transferase activator-transferase complex]]
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Current revision

Structure of E. cuniculi Mtq2-Trm112 complex responible for the methylation of eRF1 translation termination factor

PDB ID 3q87

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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